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J. Biol. Chem., Vol. 276, Issue 41, 38002-38009, October 12, 2001
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From the The pyrG gene of Lactococcus
lactis subsp. cremoris, encoding CTP synthase, has
been cloned and sequenced. It is flanked upstream by an open reading
frame showing homology to several aminotransferases and downstream by
an open reading frame of unknown function. L. lactis
strains harboring disrupted pyrG alleles were constructed. These mutants required cytidine for growth, proving that in L. lactis, the pyrG product is the only enzyme
responsible for the amination of UTP to CTP. In contrast to the
situation in Escherichia coli, an L. lactis
pyrG mutant could be constructed in the presence of a functional
cdd gene encoding cytidine deaminase. A characterization of
the enzyme revealed similar properties as found for CTP synthases from
other organisms. However, unlike the majority of CTP synthases the
lactococcal enzyme can convert dUTP to dCTP, although a half saturation
concentration of 0.6 mM for dUTP makes it unlikely that
this reaction plays a significant physiological role. As for other CTP
synthases, the oligomeric structure of the lactococcal enzyme was found
to be a tetramer, but unlike most of the other previously characterized
enzymes, the tetramer was very stable even at dilute enzyme concentrations.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ010153.
Cloning and Verification of the Lactococcus lactis
pyrG Gene and Characterization of the Gene Product, CTP
Synthase*
,,,
, and Department of Microbiology, Technical
University of Denmark, Building 301, DK-2800 Lyngby, the
§ Centre for Crystallographic Studies, Department of
Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100
Copenhagen Ø, and the Department of Biological Chemistry,
Institute of Molecular Biology, University of Copenhagen, Sølvgade
83H, DK-1307 Copenhagen, Denmark
*
This work was supported by the Danish National Research
Foundation and the Danish Government Program for Food Science and Technology through the Center for Advanced Food Studies.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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